EIF4E Antibody Cat

Total Page：16

File Type：pdf, Size：1020Kb

EIF4E Antibody Cat. No.: 60-600 EIF4E Antibody Formalin-fixed and paraffin-embedded human breast carcinoma reacted with EIF4E antibody (N-term), which was peroxidase- conjugated to the secondary antibody, followed by DAB staining. Specifications HOST SPECIES: Rabbit SPECIES REACTIVITY: Human Predicted species reactivity based on immunogen sequence: Zebrafish, Bovine, Mouse, HOMOLOGY: Rabbit, Rat, Xenopus This EIF4E antibody is generated from rabbits immunized with a KLH conjugated synthetic IMMUNOGEN: peptide between 32-61 amino acids from the N-terminal region of human EIF4E. TESTED APPLICATIONS: IHC-P, WB For WB starting dilution is: 1:1000 APPLICATIONS: For IHC-P starting dilution is: 1:50~100 September 27, 2021 1 https://www.prosci-inc.com/eif4e-antibody-60-600.html PREDICTED MOLECULAR 25 kDa WEIGHT: Properties This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by PURIFICATION: dialysis CLONALITY: Polyclonal ISOTYPE: Rabbit Ig CONJUGATE: Unconjugated PHYSICAL STATE: Liquid BUFFER: Supplied in PBS with 0.09% (W/V) sodium azide. CONCENTRATION: batch dependent Store at 4˚C for three months and -20˚C, stable for up to one year. As with all antibodies STORAGE CONDITIONS: care should be taken to avoid repeated freeze thaw cycles. Antibodies should not be exposed to prolonged high temperatures. Additional Info OFFICIAL SYMBOL: EIF4E Eukaryotic translation initiation factor 4E, eIF-4E, eIF4E, eIF-4F 25 kDa subunit, mRNA cap- ALTERNATE NAMES: binding protein, EIF4E, EIF4EL1, EIF4F ACCESSION NO.: P06730 PROTEIN GI NO.: 1352435 GENE ID: 1977 USER NOTE: Optimal dilutions for each application to be determined by the researcher. Background and References eIF4F is a multi-subunit complex, the composition of which varies with external and internal environmental conditions. It is composed of at least EIF4A, EIF4E and EIF4G1/EIF4G3. EIF4E is also known to interact with other partners. The interaction with EIF4ENIF1 mediates the import into the nucleus. Nonphosphorylated EIF4EBP1, EIF4EBP2 BACKGROUND: and EIF4EBP3 compete with EIF4G1/EIF4G3 to interact with EIF4E; insulin stimulated MAP- kinase (MAPK1 and MAPK3) phosphorylation of EIF4EBP1 causes dissociation of the complex allowing EIF4G1/EIF4G3 to bind and consequent initiation of translation. Rapamycin can attenuate insulin stimulation, mediated by FKBPs. this gene also interacts mutually exclusive with EIF4A1 and EIF4A2. REFERENCES: 1) Rychlik,W., J. Biol. Chem. 262 (22), 10434-10437 (1987) September 27, 2021 2 https://www.prosci-inc.com/eif4e-antibody-60-600.html 2) Dorfman,J., Genomics(4), 785-788 (1991) 3) Pelletier,J., Genomics 10 (4), 1079-1082 (1991) 4) Whalen,S.G., J. Biol. Chem. 271 (20), 11831-11837 (1996) ANTIBODIES FOR RESEARCH USE ONLY. For additional information, visit ProSci's Terms & Conditions Page. September 27, 2021 3 https://www.prosci-inc.com/eif4e-antibody-60-600.html.

Copy Link

Recommended publications

A Computational Approach for Defining a Signature of Β-Cell Golgi Stress in Diabetes Mellitus
Page 1 of 781 Diabetes A Computational Approach for Defining a Signature of β-Cell Golgi Stress in Diabetes Mellitus Robert N. Bone1,6,7, Olufunmilola Oyebamiji2, Sayali Talware2, Sharmila Selvaraj2, Preethi Krishnan3,6, Farooq Syed1,6,7, Huanmei Wu2, Carmella Evans-Molina 1,3,4,5,6,7,8* Departments of 1Pediatrics, 3Medicine, 4Anatomy, Cell Biology & Physiology, 5Biochemistry & Molecular Biology, the 6Center for Diabetes & Metabolic Diseases, and the 7Herman B. Wells Center for Pediatric Research, Indiana University School of Medicine, Indianapolis, IN 46202; 2Department of BioHealth Informatics, Indiana University-Purdue University Indianapolis, Indianapolis, IN, 46202; 8Roudebush VA Medical Center, Indianapolis, IN 46202. *Corresponding Author(s): Carmella Evans-Molina, MD, PhD ([email protected]) Indiana University School of Medicine, 635 Barnhill Drive, MS 2031A, Indianapolis, IN 46202, Telephone: (317) 274-4145, Fax (317) 274-4107 Running Title: Golgi Stress Response in Diabetes Word Count: 4358 Number of Figures: 6 Keywords: Golgi apparatus stress, Islets, β cell, Type 1 diabetes, Type 2 diabetes 1 Diabetes Publish Ahead of Print, published online August 20, 2020 Diabetes Page 2 of 781 ABSTRACT The Golgi apparatus (GA) is an important site of insulin processing and granule maturation, but whether GA organelle dysfunction and GA stress are present in the diabetic β-cell has not been tested. We utilized an informatics-based approach to develop a transcriptional signature of β-cell GA stress using existing RNA sequencing and microarray datasets generated using human islets from donors with diabetes and islets where type 1(T1D) and type 2 diabetes (T2D) had been modeled ex vivo. To narrow our results to GA-specific genes, we applied a filter set of 1,030 genes accepted as GA associated.
[Show full text]
Genes with 5' Terminal Oligopyrimidine Tracts Preferentially Escape Global Suppression of Translation by the SARS-Cov-2 NSP1 Protein
Downloaded from rnajournal.cshlp.org on September 28, 2021 - Published by Cold Spring Harbor Laboratory Press Genes with 5′ terminal oligopyrimidine tracts preferentially escape global suppression of translation by the SARS-CoV-2 Nsp1 protein Shilpa Raoa, Ian Hoskinsa, Tori Tonna, P. Daniela Garciaa, Hakan Ozadama, Elif Sarinay Cenika, Can Cenika,1 a Department of Molecular Biosciences, University of Texas at Austin, Austin, TX 78712, USA 1Corresponding author: [email protected] Key words: SARS-CoV-2, Nsp1, MeTAFlow, translation, ribosome profiling, RNA-Seq, 5′ TOP, Ribo-Seq, gene expression 1 Downloaded from rnajournal.cshlp.org on September 28, 2021 - Published by Cold Spring Harbor Laboratory Press Abstract Viruses rely on the host translation machinery to synthesize their own proteins. Consequently, they have evolved varied mechanisms to co-opt host translation for their survival. SARS-CoV-2 relies on a non-structural protein, Nsp1, for shutting down host translation. However, it is currently unknown how viral proteins and host factors critical for viral replication can escape a global shutdown of host translation. Here, using a novel FACS-based assay called MeTAFlow, we report a dose-dependent reduction in both nascent protein synthesis and mRNA abundance in cells expressing Nsp1. We perform RNA-Seq and matched ribosome profiling experiments to identify gene-specific changes both at the mRNA expression and translation level. We discover that a functionally-coherent subset of human genes are preferentially translated in the context of Nsp1 expression. These genes include the translation machinery components, RNA binding proteins, and others important for viral pathogenicity. Importantly, we uncovered a remarkable enrichment of 5′ terminal oligo-pyrimidine (TOP) tracts among preferentially translated genes.
[Show full text]
Early Growth Response 1 Regulates Hematopoietic Support and Proliferation in Human Primary Bone Marrow Stromal Cells
Hematopoiesis SUPPLEMENTARY APPENDIX Early growth response 1 regulates hematopoietic support and proliferation in human primary bone marrow stromal cells Hongzhe Li, 1,2 Hooi-Ching Lim, 1,2 Dimitra Zacharaki, 1,2 Xiaojie Xian, 2,3 Keane J.G. Kenswil, 4 Sandro Bräunig, 1,2 Marc H.G.P. Raaijmakers, 4 Niels-Bjarne Woods, 2,3 Jenny Hansson, 1,2 and Stefan Scheding 1,2,5 1Division of Molecular Hematology, Department of Laboratory Medicine, Lund University, Lund, Sweden; 2Lund Stem Cell Center, Depart - ment of Laboratory Medicine, Lund University, Lund, Sweden; 3Division of Molecular Medicine and Gene Therapy, Department of Labora - tory Medicine, Lund University, Lund, Sweden; 4Department of Hematology, Erasmus MC Cancer Institute, Rotterdam, the Netherlands and 5Department of Hematology, Skåne University Hospital Lund, Skåne, Sweden ©2020 Ferrata Storti Foundation. This is an open-access paper. doi:10.3324/haematol. 2019.216648 Received: January 14, 2019. Accepted: July 19, 2019. Pre-published: August 1, 2019. Correspondence: STEFAN SCHEDING - [email protected] Li et al.: Supplemental data 1. Supplemental Materials and Methods BM-MNC isolation Bone marrow mononuclear cells (BM-MNC) from BM aspiration samples were isolated by density gradient centrifugation (LSM 1077 Lymphocyte, PAA, Pasching, Austria) either with or without prior incubation with RosetteSep Human Mesenchymal Stem Cell Enrichment Cocktail (STEMCELL Technologies, Vancouver, Canada) for lineage depletion (CD3, CD14, CD19, CD38, CD66b, glycophorin A). BM-MNCs from fetal long bones and adult hip bones were isolated as reported previously 1 by gently crushing bones (femora, tibiae, fibulae, humeri, radii and ulna) in PBS+0.5% FCS subsequent passing of the cell suspension through a 40-µm filter.
[Show full text]
Mtorc1 Controls Mitochondrial Activity and Biogenesis Through 4E-BP-Dependent Translational Regulation
Cell Metabolism Article mTORC1 Controls Mitochondrial Activity and Biogenesis through 4E-BP-Dependent Translational Regulation Masahiro Morita,1,2 Simon-Pierre Gravel,1,2 Vale´ rie Che´ nard,1,2 Kristina Sikstro¨ m,3 Liang Zheng,4 Tommy Alain,1,2 Valentina Gandin,5,7 Daina Avizonis,2 Meztli Arguello,1,2 Chadi Zakaria,1,2 Shannon McLaughlan,5,7 Yann Nouet,1,2 Arnim Pause,1,2 Michael Pollak,5,6,7 Eyal Gottlieb,4 Ola Larsson,3 Julie St-Pierre,1,2,* Ivan Topisirovic,5,7,* and Nahum Sonenberg1,2,* 1Department of Biochemistry 2Goodman Cancer Research Centre McGill University, Montreal, QC H3A 1A3, Canada 3Department of Oncology-Pathology, Karolinska Institutet, Stockholm, 171 76, Sweden 4Cancer Research UK, The Beatson Institute for Cancer Research, Switchback Road, Glasgow G61 1BD, Scotland, UK 5Lady Davis Institute for Medical Research 6Cancer Prevention Center, Sir Mortimer B. Davis-Jewish General Hospital McGill University, Montreal, QC H3T 1E2, Canada 7Department of Oncology, McGill University, Montreal, QC H2W 1S6, Canada *Correspondence: [email protected] (J.S.-P.), [email protected] (I.T.), [email protected] (N.S.) http://dx.doi.org/10.1016/j.cmet.2013.10.001 SUMMARY ATP under physiological conditions in mammals and play a crit- ical role in overall energy balance (Vander Heiden et al., 2009). mRNA translation is thought to be the most energy- The mechanistic/mammalian target of rapamycin (mTOR) is a consuming process in the cell. Translation and serine/threonine kinase that has been implicated in a variety of energy metabolism are dysregulated in a variety of physiological processes and pathological states (Zoncu et al., diseases including cancer, diabetes, and heart 2011).
[Show full text]
Download Product Insert (PDF)
PRODUCT INFORMATION eIF4E (human recombinant) Item No. 15137 Overview and Properties Synonyms: eIF-4F 25 kDa subunit, Eukaryotic Translation Initiation Factor 4E, mRNA Cap-binding Protein Source: Recombinant protein expressed in E. coli Amino Acids: 2-217 (full length) Uniprot No.: P06730 Molecular Weight: 25.2 kDa Storage: -80°C (as supplied) Stability: ≥1 year Purity: batch specific (≥55% estimated by SDS-PAGE) Supplied in: 20 mM HEPES, pH 7.5, containing 100 mM potassium chloride, 2 mM DTT, and 10% glycerol Protein Concentration: batch specific mg/ml Image 1 2 3 4 250 kDa · · · · · · · 150 kDa · · · · · · · 100 kDa · · · · · · · 75 kDa · · · · · · · 50 kDa · · · · · · · 37 kDa · · · · · · · 25 kDa · · · · · · · 20 kDa · · · · · · · 15 kDa · · · · · · · Lane 1: MW Markers Lane 2: eIF4E (human recombinant) (4 µg) Lane 3: eIF4E (human recombinant) (2 µg) Lane 4: eIF4E (human recombinant) (1 µg) Representaõve gel image shown; actual purity may vary between each batch. WARNING CAYMAN CHEMICAL THIS PRODUCT IS FOR RESEARCH ONLY - NOT FOR HUMAN OR VETERINARY DIAGNOSTIC OR THERAPEUTIC USE. 1180 EAST ELLSWORTH RD SAFETY DATA ANN ARBOR, MI 48108 · USA This material should be considered hazardous until further information becomes available. Do not ingest, inhale, get in eyes, on skin, or on clothing. Wash thoroughly after handling. Before use, the user must review the complete Safety Data Sheet, which has been sent via email to your institution. PHONE: [800] 364-9897 WARRANTY AND LIMITATION OF REMEDY [734] 971-3335 Buyer agrees to purchase the material subject to Cayman’s Terms and Conditions. Complete Terms and Conditions including Warranty and Limitation of Liability information can be found on our website.
[Show full text]
Polyubiquitin Gene Ubb Is Required for Upregulation of Piwi Protein Level During Mouse Testis Development
www.nature.com/cddiscovery ARTICLE OPEN Polyubiquitin gene Ubb is required for upregulation of Piwi protein level during mouse testis development 1,4 2,4 2 1 1 2 ✉ Bitnara Han , Byung-Kwon✉ Jung , So-Hyun Park , Kyu Jin Song , Muhammad Ayaz Anwar , Kwon-Yul Ryu and Kwang Pyo Kim 1,3 © The Author(s) 2021 Testis development, including early embryonic gonad formation and late postnatal spermatogenesis, is essential for the reproduction of higher metazoans to generate fertile gametes, called sperm. We have previously reported that the polyubiquitin gene Ubb is required for fertility in both male and female mice. In particular, the Ubb-null male mice showed an azoospermia phenotype due to arrest of spermatogenesis at the pachytene stage. Here, we analyzed the whole testis proteome at postnatal day 20 to define the molecular mediators of the male-infertility phenotype caused by Ubb knockout. From the identified proteome, 564 proteins were significantly and differentially expressed in Ubb-knockout testes and, among these, 36 downregulated proteins were involved at different stages of spermatogenesis. We also found that levels of piRNA metabolic process-related proteins, including Piwil2 and Tdrd1, were downregulated in Ubb-null testes through functional gene ontology analysis. Further, protein–protein interaction mapping revealed that 24 testis development-related proteins, including Hsp90aa1, Eef1a1, and Pabpc1, were directly influenced by the depletion of ubiquitin. In addition, the reduced mRNA levels of these proteins were observed in Ubb-knockout testes, which closely resembled the global downregulation of piRNA-metabolic gene expression at the transcriptional and post- transcriptional levels. Together with proteomic and transcriptional analyses, our data suggest that Ubb expression is essential for the maintenance of testicular RNA-binding regulators and piRNA-metabolic proteins to complete spermatogenesis in mice.
[Show full text]
EIF1AX and RAS Mutations Cooperate to Drive Thyroid Tumorigenesis Through ATF4 and C-MYC
Published OnlineFirst October 10, 2018; DOI: 10.1158/2159-8290.CD-18-0606 RESEARCH ARTICLE EIF1AX and RAS Mutations Cooperate to Drive Thyroid Tumorigenesis through ATF4 and c-MYC Gnana P. Krishnamoorthy 1 , Natalie R. Davidson 2 , Steven D. Leach 1 , Zhen Zhao 3 , Scott W. Lowe 3 , Gina Lee 4 , Iňigo Landa 1 , James Nagarajah 1 , Mahesh Saqcena 1 , Kamini Singh 3 , Hans-Guido Wendel3 , Snjezana Dogan 5 , Prasanna P. Tamarapu 1 , John Blenis 4 , Ronald A. Ghossein 5 , Jeffrey A. Knauf 1 , 6 , Gunnar Rätsch 2 , and James A. Fagin 1 , 6 ABSTRACT Translation initiation is orchestrated by the cap binding and 43S preinitiation com- plexes (PIC). Eukaryotic initiation factor 1A (EIF1A) is essential for recruitment of the ternary complex and for assembling the 43S PIC. Recurrent EIF1AX mutations in papillary thyroid cancers are mutually exclusive with other drivers, including RAS . EIF1AX mutations are enriched in advanced thyroid cancers, where they display a striking co-occurrence with RAS , which cooperates to induce tumorigenesis in mice and isogenic cell lines. The C-terminal EIF1AX-A113splice mutation is the most prevalent in advanced thyroid cancer. EIF1AX-A113splice variants stabilize the PIC and induce ATF4, a sensor of cellular stress, which is co-opted to suppress EIF2α phosphorylation, enabling a gen- eral increase in protein synthesis. RAS stabilizes c-MYC, an effect augmented by EIF1AX-A113splice. ATF4 and c-MYC induce expression of amino acid transporters and enhance sensitivity of mTOR to amino acid supply. These mutually reinforcing events generate therapeutic vulnerabilities to MEK, BRD4, and mTOR kinase inhibitors. SIGNIFICANCE: Mutations of EIF1AX, a component of the translation PIC, co-occur with RAS in advanced thyroid cancers and promote tumorigenesis.
[Show full text]
Beyond Traditional Morphological Characterization of Lung
Cancers 2020 S1 of S15 Beyond Traditional Morphological Characterization of Lung Neuroendocrine Neoplasms: In Silico Study of Next-Generation Sequencing Mutations Analysis across the Four World Health Organization Defined Groups Giovanni Centonze, Davide Biganzoli, Natalie Prinzi, Sara Pusceddu, Alessandro Mangogna, Elena Tamborini, Federica Perrone, Adele Busico, Vincenzo Lagano, Laura Cattaneo, Gabriella Sozzi, Luca Roz, Elia Biganzoli and Massimo Milione Table S1. Genes Frequently mutated in Typical Carcinoids (TCs). Mutation Original Entrez Gene Gene Rate % eukaryotic translation initiation factor 1A X-linked [Source: HGNC 4.84 EIF1AX 1964 EIF1AX Symbol; Acc: HGNC: 3250] AT-rich interaction domain 1A [Source: HGNC Symbol;Acc: HGNC: 4.71 ARID1A 8289 ARID1A 11110] LDL receptor related protein 1B [Source: HGNC Symbol; Acc: 4.35 LRP1B 53353 LRP1B HGNC: 6693] 3.53 NF1 4763 NF1 neurofibromin 1 [Source: HGNC Symbol;Acc: HGNC: 7765] DS cell adhesion molecule like 1 [Source: HGNC Symbol; Acc: 2.90 DSCAML1 57453 DSCAML1 HGNC: 14656] 2.90 DST 667 DST dystonin [Source: HGNC Symbol;Acc: HGNC: 1090] FA complementation group D2 [Source: HGNC Symbol; Acc: 2.90 FANCD2 2177 FANCD2 HGNC: 3585] piccolo presynaptic cytomatrix protein [Source: HGNC Symbol; Acc: 2.90 PCLO 27445 PCLO HGNC: 13406] erb-b2 receptor tyrosine kinase 2 [Source: HGNC Symbol; Acc: 2.44 ERBB2 2064 ERBB2 HGNC: 3430] BRCA1 associated protein 1 [Source: HGNC Symbol; Acc: HGNC: 2.35 BAP1 8314 BAP1 950] capicua transcriptional repressor [Source: HGNC Symbol; Acc: 2.35 CIC 23152 CIC HGNC:
[Show full text]
Drosophila and Human Transcriptomic Data Mining Provides Evidence for Therapeutic
Drosophila and human transcriptomic data mining provides evidence for therapeutic mechanism of pentylenetetrazole in Down syndrome Author Abhay Sharma Institute of Genomics and Integrative Biology Council of Scientific and Industrial Research Delhi University Campus, Mall Road Delhi 110007, India Tel: +91-11-27666156, Fax: +91-11-27662407 Email: [email protected] Nature Precedings : hdl:10101/npre.2010.4330.1 Posted 5 Apr 2010 Running head: Pentylenetetrazole mechanism in Down syndrome 1 Abstract Pentylenetetrazole (PTZ) has recently been found to ameliorate cognitive impairment in rodent models of Down syndrome (DS). The mechanism underlying PTZ’s therapeutic effect is however not clear. Microarray profiling has previously reported differential expression of genes in DS. No mammalian transcriptomic data on PTZ treatment however exists. Nevertheless, a Drosophila model inspired by rodent models of PTZ induced kindling plasticity has recently been described. Microarray profiling has shown PTZ’s downregulatory effect on gene expression in fly heads. In a comparative transcriptomics approach, I have analyzed the available microarray data in order to identify potential mechanism of PTZ action in DS. I find that transcriptomic correlates of chronic PTZ in Drosophila and DS counteract each other. A significant enrichment is observed between PTZ downregulated and DS upregulated genes, and a significant depletion between PTZ downregulated and DS dowwnregulated genes. Further, the common genes in PTZ Nature Precedings : hdl:10101/npre.2010.4330.1 Posted 5 Apr 2010 downregulated and DS upregulated sets show enrichment for MAP kinase pathway. My analysis suggests that downregulation of MAP kinase pathway may mediate therapeutic effect of PTZ in DS. Existing evidence implicating MAP kinase pathway in DS supports this observation.
[Show full text]
Global Analysis of LARP1 Translation Targets Reveals Tunable and Dynamic Features of 5′ TOP Motifs
Global analysis of LARP1 translation targets reveals tunable and dynamic features of 5′ TOP motifs Lucas Philippea,1, Antonia M. G. van den Elzena,1, Maegan J. Watsona, and Carson C. Thoreena,2 aDepartment of Cellular and Molecular Physiology, Yale School of Medicine, New Haven, CT 06510 Edited by Alan G. Hinnebusch, National Institutes of Health, Bethesda, MD, and approved January 29, 2020 (received for review July 25, 2019) Terminal oligopyrimidine (TOP) motifs are sequences at the 5′ ends recent findings have hinted that the RNA-binding protein La- of mRNAs that link their translation to the mTOR Complex 1 related protein 1 (LARP1) may have a central role (8–10). (mTORC1) nutrient-sensing signaling pathway. They are com- LARP1 is a large protein (150 kDa) with several RNA-binding monly regarded as discrete elements that reside on ∼100 mRNAs domains. Its central region contains a La motif (LaM) domain that mostly encode translation factors. However, the full spectrum that defines the La-related protein (LARP) superfamily, along of TOP sequences and their prevalence throughout the transcrip- with an adjacent RNA recognition motif-like (RRM-L) domain. tome remain unclear, primarily because of uncertainty over the Its C terminus encodes a domain known as the DM15 region. This mechanism that detects them. Here, we globally analyzed trans- domain is unique to LARP1 and its closely related homolog lation targets of La-related protein 1 (LARP1), an RNA-binding pro- LARP1B, and is therefore also known as the LARP1 domain (11). tein and mTORC1 effector that has been shown to repress TOP Several observations suggest that LARP1 directly represses TOP mRNA translation in a few specific cases.
[Show full text]
Relevance of Translation Initiation in Diffuse Glioma Biology and Its
cells Review Relevance of Translation Initiation in Diﬀuse Glioma Biology and its Therapeutic Potential Digregorio Marina 1, Lombard Arnaud 1,2, Lumapat Paul Noel 1, Scholtes Felix 1,2, Rogister Bernard 1,3 and Coppieters Natacha 1,* 1 Laboratory of Nervous System Disorders and Therapy, GIGA-Neurosciences Research Centre, University of Liège, 4000 Liège, Belgium; [email protected] (D.M.); [email protected] (L.A.); [email protected] (L.P.N.); [email protected] (S.F.); [email protected] (R.B.) 2 Department of Neurosurgery, CHU of Liège, 4000 Liège, Belgium 3 Department of Neurology, CHU of Liège, 4000 Liège, Belgium * Correspondence: [email protected] Received: 18 October 2019; Accepted: 26 November 2019; Published: 29 November 2019 Abstract: Cancer cells are continually exposed to environmental stressors forcing them to adapt their protein production to survive. The translational machinery can be recruited by malignant cells to synthesize proteins required to promote their survival, even in times of high physiological and pathological stress. This phenomenon has been described in several cancers including in gliomas. Abnormal regulation of translation has encouraged the development of new therapeutics targeting the protein synthesis pathway. This approach could be meaningful for glioma given the fact that the median survival following diagnosis of the highest grade of glioma remains short despite current therapy. The identiﬁcation of new targets for the development of novel therapeutics is therefore needed in order to improve this devastating overall survival rate. This review discusses current literature on translation in gliomas with a focus on the initiation step covering both the cap-dependent and cap-independent modes of initiation.
[Show full text]
ERK5 Binding Partners
Supplementary Table 1: ERK5 binding partners id Protein IDs Protein namesGene namesRazor + uniqueSequence peptides coverageLFQ intensity [%]LFQ FL_m_01 intensityLFQ FL_m_02 intensityLFQ FL_m_03 intensityLFQ FL_p_01 intensityLFQ FL_p_02 intensityLFQ FL_p_03 intensityLFQ MU_p_01 intensityLFQ MU_p_02 intensitynormalized MU_p_03 normalizedLog2 IFL_m_01 normalizedLog2 IFL_m_02 normalizedLog2 IFL_m_03 normalizedLog2 IFL_p_01 normalizedLog2 IFL_p_02 normalizedLog2 IFL_p_03 normalizedLog2 IMU_p_01 normalizedLog2 IMU_p_02 medianLog2 IMU_p_03 - mediam FL median Mutst dev - st dev fl st dev mut cluster1 cluster2 cluster3 950 H7BXZ6 MitochondrialRHOT1 Rho GTPase 2 6.5 1.08E+08 26.77 26.77 + 405 B7WPL0 Synembryn-BRIC8B 2 6.1 9.55E+07 26.75 26.75 + 780 F6RFD5 Destrin DSTN 5 37.8 3.94E+07 25.49 25.49 + 360 B1AN48 Small proline-richSPRR3 protein 3 2 10.1 3.65E+07 25.24 25.24 + 1376 P02808 Statherin STATH 2 54.8 3.05E+07 25.12 25.12 + 196 A0A0A0MTI6Elongation ofELOVL5 very long chain fatty2 acids protein8.4 1.92E+07 1.52E+07 24.35 24.09 24.22 0.188066 + 2157 Q13163-4 Dual specificityMAP2K5 mitogen-activated6 protein18.7 kinase kinase 5 9.04E+06 2.09E+07 1.04E+07 8.78E+06 1.28E+07 1.06E+07 23.11 24.49 23.53 23.01 23.4 22.9 23.53 23.01 0.704014 0.263334 + 2702 Q96AB3-3 IsochorismataseISOC2 domain-containing2 protein28.1 2, mitochondrial 8.02E+06 23.1 23.1 + 64 A0A087WW54DEP domain-containingDEPDC7 protein 75 9.6 4.88E+06 7.56E+06 1.20E+07 3.13E+06 22.21 23.03 23.69 21.54 23.03 21.54 0.742829 + 1673 P30837 Aldehyde dehydrogenaseALDH1B1 X, mitochondrial5 13.7
[Show full text]